ArticleJournal of bacteriology2005
Mutations in cytochrome assembly and periplasmic redox pathways in Bordetella pertussis.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- Analysis of putative heme ligands in the System I bacterial cytochromeMicrobiology spectrum · 2026Article
- Helicobacter pylori and Campylobacter jejuni bacterial holocytochrome c synthase structure-function analysis reveals conservation of heme binding.Communications biology · 2024Article
- Structural basis of membrane machines that traffick and attach heme to cytochromes.The Journal of biological chemistry · 2023Article
- Article
- CCS2, an Octatricopeptide-Repeat Protein, Is Required for Plastid CytochromeFrontiers in plant science · 2017Article
- An easy and efficient permeabilization protocol for in vivo enzyme activity assays in cyanobacteria.Microbial cell factories · 2016Article
- Auxenochlorella protothecoides and Prototheca wickerhamii plastid genome sequences give insight into the origins of non-photosynthetic algae.Scientific reports · 2015Article
- Diversity of the Epsilonproteobacteria Dsb (disulfide bond) systems.Frontiers in microbiology · 2015Review
- Protein Machineries Involved in the Attachment of Heme to Cytochrome c: Protein Structures and Molecular Mechanisms.Scientifica · 2013Review
- Thiol redox requirements and substrate specificities of recombinant cytochrome c assembly systems II and III.Biochimica et biophysica acta · 2012Article
- Characterization of DsbD in Neisseria meningitidis.Molecular microbiology · 2011Article
- A novel component of the disulfide-reducing pathway required for cytochrome c assembly in plastids.Genetics · 2011Article
- Role of heme and heme-proteins in trypanosomatid essential metabolic pathways.Enzyme research · 2011Article
- c-type cytochrome assembly in Saccharomyces cerevisiae: a key residue for apocytochrome c1/lyase interaction.Genetics · 2010Article
- CCS5, a thioredoxin-like protein involved in the assembly of plastid c-type cytochromes.The Journal of biological chemistry · 2010Article
- Substrate specificity of three cytochrome c haem lyase isoenzymes from Wolinella succinogenes: unconventional haem c binding motifs are not sufficient for haem c attachment by NrfI and CcsA1.Molecular microbiology · 2010Article
- Cytochrome c biogenesis: mechanisms for covalent modifications and trafficking of heme and for heme-iron redox control.Microbiology and molecular biology reviews : MMBR · 2009Review
- CcsBA is a cytochrome c synthetase that also functions in heme transport.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Topology and function of CcmD in cytochrome c maturation.Journal of bacteriology · 2008Article
- Heme concentration dependence and metalloporphyrin inhibition of the system I and II cytochrome c assembly pathways.Journal of bacteriology · 2007Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Transposon mutagenesis of Bordetella pertussis was used to discover mutations in the cytochrome c biogenesis pathway called system II. Using a tetramethyl-p-phenylenediamine cytochrome c oxidase screen, 27 oxidase-negative mutants were isolated and characterized. Nine mutants were still able to synthesize c-type cytochromes and possessed insertions in the genes for cytochrome c oxidase subunits (ctaC, -D, and -E), heme a biosynthesis (ctaB), assembly of cytochrome c oxidase (sco2), or ferrochelatase (hemZ). Eighteen mutants were unable to synthesize all c-type cytochromes. Seven of these had transposons in dipZ (dsbD), encoding the transmembrane thioreduction protein, and all seven mutants were corrected for cytochrome c assembly by exogenous dithiothreitol, which was consistent with the cytochrome c cysteinyl residues of the CXXCH motif requiring periplasmic reduction. The remaining 11 insertions were located in the ccsBA operon, suggesting that with the appropriate thiol-reducing environment, the CcsB and CcsA proteins comprise the entire system II biosynthetic pathway. Antiserum to CcsB was used to show that CcsB is absent in ccsA mutants, providing evidence for a stable CcsA-CcsB complex. No mutations were found in the genes necessary for disulfide bond formation (dsbA or dsbB). To examine whether the periplasmic disulfide bond pathway is required for cytochrome c biogenesis in B. pertussis, a targeted knockout was made in dsbB. The DsbB- mutant makes holocytochromes c like the wild type does and secretes and assembles the active periplasmic alkaline phosphatase. A dipZ mutant is not corrected by a dsbB mutation. Alternative mechanisms to oxidize disulfides in B. pertussis are analyzed and discussed.
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